8SAB
Crystal Structure of Cystathionine beta lyase from Klebsiella aerogenes, PLP adduct with Alanine (C2 form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-02-14 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9795 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 87.325, 130.522, 82.366 |
Unit cell angles | 90.00, 103.96, 90.00 |
Refinement procedure
Resolution | 34.180 - 1.600 |
R-factor | 0.1602 |
Rwork | 0.159 |
R-free | 0.18170 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.772 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.21rc1_4918: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 79.930 | 1.640 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.091 | 1.036 |
Rmeas | 0.100 | 1.136 |
Rpim | 0.041 | 0.462 |
Total number of observations | 667211 | 50244 |
Number of reflections | 116919 | 8555 |
<I/σ(I)> | 11.7 | 1.9 |
Completeness [%] | 99.5 | |
Redundancy | 5.7 | 5.9 |
CC(1/2) | 0.999 | 0.659 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | Morpueus H12: 12.5%(v/v) MPD, 12.5%(v/v) PEG 1000, 12.5%(w/v) PEG 3350, 100 mM Tris/BICINE, pH 8.5, 20 mM DL-Glutamic acid, 20 mM DL-Alanine; 20 mM Glycine, 20 mM DL-Lysine monohydrochloride and 20 mM DL-Serine. 2mM PLP and 2mM Arginine added to protein prior to crystallization, KlaeA.00906.a.B1.PW39169 at 41.1 mg/mL. Plate: 13220 well H12 drop 3, Puck: PSL-0506, Cryo: Direct |